Results 311 to 320 of about 146,694 (331)
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2014
Many microbial pathogens are known to possess heme acquisition systems that allow the organisms to utilize heme or heme-bound proteins as sources of iron. These systems have been demonstrated to procure iron from heme, hemoglobin, haptoglobin, or hemopexin and are identified as nonsiderophore heme iron acquisition systems.
Melanie Ratliff-Griffin +2 more
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Many microbial pathogens are known to possess heme acquisition systems that allow the organisms to utilize heme or heme-bound proteins as sources of iron. These systems have been demonstrated to procure iron from heme, hemoglobin, haptoglobin, or hemopexin and are identified as nonsiderophore heme iron acquisition systems.
Melanie Ratliff-Griffin +2 more
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Heme oxygenase-1 as a target for drug discovery.
Antioxidants and Redox Signaling, 2014SIGNIFICANCE Heme oxygenase enzymes, which exist as constitutive (HO-2) and inducible (HO-1) isoforms, degrade heme to carbon monoxide (CO) and the bile pigment biliverdin.
R. Motterlini, R. Foresti
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2005
The heme oxygenase (HO) system is the rate-limiting step in the conversion of heme into biliverdin, carbon monoxide (CO) and free iron (Fe). This oxidation reaction involves a sequence of transformations that consumes three molecules of O2 and seven electrons. In mammals, the electrons are provided by NADPH-cytochrome-P-450 reductase. Three HO isoforms
Jerzy W. Kupiec-Weglinski +2 more
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The heme oxygenase (HO) system is the rate-limiting step in the conversion of heme into biliverdin, carbon monoxide (CO) and free iron (Fe). This oxidation reaction involves a sequence of transformations that consumes three molecules of O2 and seven electrons. In mammals, the electrons are provided by NADPH-cytochrome-P-450 reductase. Three HO isoforms
Jerzy W. Kupiec-Weglinski +2 more
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Expression of Heme Oxygenase in Hemopoiesis
1988Heme oxygenase has been purified to electrophoretic homogeneity from detergent solubilized adult human liver microsomes. Treatment of microsomes with Triton X-100, sodium cholate and subsequent batchwise DEAE-cellulose, 2', 5' ADP-sepharose 4B, Sepharose CLB and hydroxylapatite column resulted in 17% yield of the purified heme oxygenase.
Nader G. Abraham +5 more
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Structure and Catalytic Mechanism of Heme Oxygenase
ChemInform, 2007AbstractChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 200 leading journals. To access a ChemInform Abstract, please click on HTML or PDF.
Toshitaka Matsui +2 more
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Purification and Characterization of Heme Oxygenase
Current Protocols in Toxicology, 2003AbstractHigh‐yield expression and purification of human heme oxygenase isozyme 1 provided the breakthrough in characterizing the protein from mechanistic and structural standpoints. This unit provides a protocol for high‐level expression and subsequent purification of HO‐1.
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Heme degradation by the microsomal heme oxygenase system
Trends in Biochemical Sciences, 1980Abstract Heme degradation in the heme oxygenase reaction proceeds essentially as an autocatalytic oxidation of heme which is bound to heme oxygenase; in this reaction heme acts as both the substrate and the coenzyme which activates molecular oxygen. Synthesis of heme oxygenase can be induced by heme itself, in a substrate-mediated induction.
Goro Kikuchi, Tadashi Yoshida
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Proceedings of the Society for Experimental Biology and Medicine, 1999
Abstract.Heme is a molecule that is synthesized by the sequential actions of eight enzymes and is ubiquitous throughout nature. For many years it has been known that heme is also catabolized to yield biliverdin (which is subsequently reduced to bilirubin), one atom of iron, and one molecule of carbon monoxide.
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Abstract.Heme is a molecule that is synthesized by the sequential actions of eight enzymes and is ubiquitous throughout nature. For many years it has been known that heme is also catabolized to yield biliverdin (which is subsequently reduced to bilirubin), one atom of iron, and one molecule of carbon monoxide.
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Function and induction of the microsomal heme oxygenase
Molecular and Cellular Biochemistry, 1983The microsomal heme oxygenase system consists of heme oxygenase and NADPH-cytochrome P-450 reductase, and is considered to play a key role in the physiological heme catabolism to yield biliverdin in animals. Heme oxygenase purified from either pig spleen or rat liver has a minimum molecular weight of 32 000, and binds heme to form a 1:1 complex which ...
Goro Kikuchi, Tadashi Yoshida
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Heme oxygenase-1 mediates BAY 11-7085 induced ferroptosis.
Cancer Letters, 2018Ling-Chu Chang +5 more
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